Abstract
Bioactive peptides play important roles in metabolic regulation and modulation and many are used as therapeutics. These peptides often possess disulfide bonds, which are important for their structure, function and stability. A systematic network of enzymes—a disulfide bond generating enzyme, a disulfide bond donor enzyme and a redox cofactor—that function inside the cell dictates the formation and maintenance of disulfide bonds. The main pathways that catalyze disulfide bond formation in peptides and proteins in prokaryotes and eukaryotes are remarkably similar and share several mechanistic features. This review summarizes the formation of disulfide bonds in peptides and proteins by cellular and recombinant machinery.
Highlights
IntroductionDisulfide bonds are common structural motifs in many bioactive peptides and proteins including hormones, neurotransmitters, growth factors, enzyme inhibitors, and antimicrobial peptides [1,2,3]
Disulfide bonds are common structural motifs in many bioactive peptides and proteins including hormones, neurotransmitters, growth factors, enzyme inhibitors, and antimicrobial peptides [1,2,3].They play a critical role in maintaining the overall fold of the peptides and proteins and are thereby often important for the function and stability of proteins and peptides
DsbA is known to have no proofreading activity and can form incorrect disulfides in proteins with multiple cysteines. These incorrect disulfide bonds are corrected by a protein disulfide isomerase, DsbC, which is kept in the reduced and active configuration by a membrane-bound protein, DsbD
Summary
Disulfide bonds are common structural motifs in many bioactive peptides and proteins including hormones, neurotransmitters, growth factors, enzyme inhibitors, and antimicrobial peptides [1,2,3]. They play a critical role in maintaining the overall fold of the peptides and proteins and are thereby often important for the function and stability of proteins and peptides. In nature, such bonds are usually formed during the posttranslational modification stage with the assistance of appropriate enzymes and co-factors whereas, in the laboratory, disulfide bonds in native proteins can be formed randomly in basic buffer via air oxidation or by regioselective methods. This review discusses biological means of disulfide bond formation in biological systems
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